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- PDB-2w55: Crystal Structure of Xanthine Dehydrogenase (E232Q variant) from ... -

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Basic information

Entry
Database: PDB / ID: 2w55
TitleCrystal Structure of Xanthine Dehydrogenase (E232Q variant) from Rhodobacter capsulatus in Complex with Hypoxanthine
Components(XANTHINE DEHYDROGENASE) x 2
KeywordsOXIDOREDUCTASE / XDH / GOUT / IRON / XANTHINE / IRON-SULFUR / MOLYBDENUM COFACTOR / HYPOXANTHINE / METAL-BINDING
Function / homology
Function and homology information


1.1.1.204 / xanthine dehydrogenase activity / molybdenum ion binding / FAD binding / 2 iron, 2 sulfur cluster binding / oxidoreductase activity / iron ion binding
Similarity search - Function
Xanthine dehydrogenase, small subunit, bacteria / Xanthine dehydrogenase, molybdopterin binding subunit / Xanthine dehydrogenase, small subunit / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead / CO dehydrogenase flavoprotein, C-terminal domain / CO dehydrogenase flavoprotein C-terminal domain / Aldehyde Oxidoreductase; domain 4 / Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain / [2Fe-2S]-binding domain / Molybdopterin dehydrogenase, FAD-binding ...Xanthine dehydrogenase, small subunit, bacteria / Xanthine dehydrogenase, molybdopterin binding subunit / Xanthine dehydrogenase, small subunit / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead / CO dehydrogenase flavoprotein, C-terminal domain / CO dehydrogenase flavoprotein C-terminal domain / Aldehyde Oxidoreductase; domain 4 / Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain / [2Fe-2S]-binding domain / Molybdopterin dehydrogenase, FAD-binding / CO dehydrogenase flavoprotein, C-terminal / CO dehydrogenase flavoprotein, C-terminal domain superfamily / FAD binding domain in molybdopterin dehydrogenase / CO dehydrogenase flavoprotein C-terminal domain / Aldehyde oxidase/xanthine dehydrogenase / Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain / Molybdopterin cofactor-binding domain / Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead / [2Fe-2S]-binding / Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily / [2Fe-2S]-binding domain superfamily / Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily / [2Fe-2S] binding domain / Molybdopterin cofactor-binding domain / Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 - #10 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 / FAD-binding, type PCMH, subdomain 1 / Aldehyde Oxidoreductase; domain 3 / 2Fe-2S ferredoxin, iron-sulphur binding site / 2Fe-2S ferredoxin-type iron-sulfur binding region signature. / FAD-binding domain, PCMH-type / PCMH-type FAD-binding domain profile. / 2Fe-2S iron-sulfur cluster binding domain / Beta-grasp domain / FAD-binding, type PCMH, subdomain 2 / FAD-binding, type PCMH-like superfamily / Beta-grasp domain superfamily / Enolase-like; domain 1 / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / Ubiquitin-like (UB roll) / DNA polymerase; domain 1 / Roll / Alpha-Beta Complex / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / HYPOXANTHINE / Chem-XAX / Xanthine dehydrogenase / Xanthine dehydrogenase
Similarity search - Component
Biological speciesRHODOBACTER CAPSULATUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsDoebbler, J.A. / Truglio, J.J. / Leimkuhler, S. / Kisker, C.
CitationJournal: J.Biol.Chem. / Year: 2009
Title: Mechanism of Substrate and Inhibitor Binding of Rhodobacter Capsulatus Xanthine Dehydrogenase.
Authors: Dietzel, U. / Kuper, J. / Doebbler, J.A. / Schulte, A. / Truglio, J.J. / Leimkuhler, S. / Kisker, C.
History
DepositionDec 4, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 23, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Apr 22, 2015Group: Atomic model / Derived calculations ...Atomic model / Derived calculations / Non-polymer description / Other
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: XANTHINE DEHYDROGENASE
B: XANTHINE DEHYDROGENASE
C: XANTHINE DEHYDROGENASE
D: XANTHINE DEHYDROGENASE
E: XANTHINE DEHYDROGENASE
F: XANTHINE DEHYDROGENASE
G: XANTHINE DEHYDROGENASE
H: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)537,45032
Polymers529,5908
Non-polymers7,86024
Water77543
1
A: XANTHINE DEHYDROGENASE
B: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,3638
Polymers132,3982
Non-polymers1,9656
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8030 Å2
ΔGint-34.9 kcal/mol
Surface area49430 Å2
MethodPQS
2
C: XANTHINE DEHYDROGENASE
D: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,3638
Polymers132,3982
Non-polymers1,9656
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7990 Å2
ΔGint-34.1 kcal/mol
Surface area49590 Å2
MethodPQS
3
E: XANTHINE DEHYDROGENASE
F: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,3638
Polymers132,3982
Non-polymers1,9656
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8210 Å2
ΔGint-34.9 kcal/mol
Surface area49690 Å2
MethodPQS
4
G: XANTHINE DEHYDROGENASE
H: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,3638
Polymers132,3982
Non-polymers1,9656
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8080 Å2
ΔGint-36.8 kcal/mol
Surface area49350 Å2
MethodPQS
Unit cell
Length a, b, c (Å)92.741, 140.568, 157.606
Angle α, β, γ (deg.)109.45, 106.10, 101.09
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
31E
41G
12B
22D
32F
42H
13B
23D
33F
43H

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUPROPRO4AA2 - 4622 - 462
21GLUGLUPROPRO4CC2 - 4622 - 462
31GLUGLUPROPRO4EE2 - 4622 - 462
41GLUGLUPROPRO4GG2 - 4622 - 462
12SERSERALAALA4BB2 - 7772 - 777
22SERSERALAALA4DD2 - 7772 - 777
32SERSERALAALA4FF2 - 7772 - 777
42SERSERALAALA4HH2 - 7772 - 777
13HPAHPAHPAHPA1BN1780
33HPAHPAHPAHPA1FZ1780
23HPAHPAHPAHPA1DT1780
43HPAHPAHPAHPA1HFA1780

NCS ensembles :
ID
1
2
3

NCS oper:
IDCodeMatrixVector
1given(-0.01845, -0.7891, 0.614), (-0.795, -0.3609, -0.4876), (0.6064, -0.4971, -0.6206)0.2342, 0.03739, -0.157
2given(0.327, -0.7158, -0.617), (0.8697, -0.02757, 0.4928), (-0.3698, -0.6978, 0.6135)89.49, -24.41, 10.54
3given(-0.9268, -0.3757, -0.001493), (-0.3757, 0.9268, -0.000154), (0.001442, 0.000418, -1)23.48, -67.02, 60.41
4given(-0.03254, -0.7883, 0.6145), (-0.7853, -0.3601, -0.5036), (0.6182, -0.499, -0.6073)-0.00545, 0.1665, 0.09686
5given(0.3338, -0.7139, -0.6156), (0.8611, -0.03473, 0.5073), (-0.3835, -0.6994, 0.6031)89.11, -24.8, 11.68
6given(-0.9268, -0.3755, -0.006569), (-0.3755, 0.9268, 0.000266), (0.005989, 0.002713, -1)23.63, -67.05, 60.34

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Components

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Protein , 2 types, 8 molecules ACEGBDFH

#1: Protein
XANTHINE DEHYDROGENASE /


Mass: 49420.508 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RHODOBACTER CAPSULATUS (bacteria) / Plasmid: PSL207 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): TP1000 / References: UniProt: O54050, 1.1.1.204
#2: Protein
XANTHINE DEHYDROGENASE /


Mass: 82977.047 Da / Num. of mol.: 4 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RHODOBACTER CAPSULATUS (bacteria) / Plasmid: PSL207 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): TP1000 / References: UniProt: O54051, 1.1.1.204

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Non-polymers , 6 types, 67 molecules

#3: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Fe2S2
#4: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#5: Chemical
ChemComp-XAX / {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-kappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(hydroxy)oxo(thioxo)molybdenum


Mass: 554.348 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H13MoN5O8PS3
#6: Chemical
ChemComp-BA / BARIUM ION


Mass: 137.327 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ba
#7: Chemical
ChemComp-HPA / HYPOXANTHINE / Hypoxanthine


Mass: 136.111 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C5H4N4O
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 43 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN B, GLU 232 TO GLN ENGINEERED RESIDUE IN CHAIN D, GLU 232 TO GLN ...ENGINEERED RESIDUE IN CHAIN B, GLU 232 TO GLN ENGINEERED RESIDUE IN CHAIN D, GLU 232 TO GLN ENGINEERED RESIDUE IN CHAIN F, GLU 232 TO GLN ENGINEERED RESIDUE IN CHAIN H, GLU 232 TO GLN
Sequence detailsE232Q VARIANT

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.35 Å3/Da / Density % sol: 63.25 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop / pH: 8.3
Details: 100 MM TRIS PH 8.3, 6-8 % PEG 8000, 6-8 MM BACL, 5-25 MM DTT, 3-4 % ISOPROPANOL, 10-15 MG/ML PROTEIN IN A 1:2 RATIO WITH THE RESERVOIR SOLUTION, HANGING DROP VAPOR DIFFUSION

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD / Details: A DOUBLY FOCUSING TOROIDAL MIRROR
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.4→50 Å / Num. obs: 83695 / % possible obs: 93.9 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 7.8
Reflection shellResolution: 3.4→3.52 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 1.9 / % possible all: 69

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Processing

Software
NameVersionClassification
REFMAC5.5.0055refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1JRO

1jro


Resolution: 3.4→50 Å / Cor.coef. Fo:Fc: 0.898 / Cor.coef. Fo:Fc free: 0.841 / SU B: 64.606 / SU ML: 0.48 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.633 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.27 4451 5 %RANDOM
Rwork0.221 ---
obs0.223 83695 93.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 43.12 Å2
Baniso -1Baniso -2Baniso -3
1-0.42 Å20.25 Å2-4.1 Å2
2---0.96 Å2-2.4 Å2
3----3.23 Å2
Refinement stepCycle: LAST / Resolution: 3.4→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms36364 0 400 43 36807
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.02237560
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0821.9751048
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.27754824
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.1522.5931620
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.007155780
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.29115368
X-RAY DIFFRACTIONr_chiral_restr0.070.25652
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02128932
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.0951.523988
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.184238108
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.327313572
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.5724.512924
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
31B10tight positional0.010.05
33F10tight positional0.010.05
32D10tight positional00.05
34H10tight positional0.010.05
11A3367medium positional0.30.5
12C3367medium positional0.310.5
13E3367medium positional0.310.5
14G3367medium positional0.30.5
21B5716medium positional0.290.5
22D5716medium positional0.290.5
23F5716medium positional0.310.5
24H5716medium positional0.290.5
31B10tight thermal0.050.5
33F10tight thermal0.030.5
32D10tight thermal0.050.5
34H10tight thermal0.040.5
11A3367medium thermal0.122
12C3367medium thermal0.172
13E3367medium thermal0.132
14G3367medium thermal0.132
21B5716medium thermal0.162
22D5716medium thermal0.182
23F5716medium thermal0.172
24H5716medium thermal0.162
LS refinement shellResolution: 3.4→3.49 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.339 223 -
Rwork0.291 4208 -
obs--64.39 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
13.8299-0.70651.01623.2386-0.55682.6209-0.07510.40170.3407-0.24050.12330.363-0.6190.0011-0.04810.2176-0.04910.00460.18650.08920.244510.121326.3447-9.5404
21.4208-0.41881.03991.45260.57193.206-0.0630.01630.5066-0.12970.05480.3719-0.6155-0.09710.00810.6303-0.0340.06990.16860.06730.65745.682252.67742.7313
30.53360.19910.17111.07770.38940.8578-0.006-0.18370.18910.17630.0609-0.1114-0.24750.1659-0.05490.1676-0.0390.0040.1931-0.0450.15717.797815.791519.0264
42.2429-0.81271.3583.3347-0.01782.4334-0.18-0.04690.219-0.0599-0.11440.3188-0.2783-0.46020.29440.03420.0512-0.04650.1985-0.06620.2193-26.8127-12.6164-0.9522
52.1503-1.45280.4414.0541.75633.01690.09110.2940.1932-0.2178-0.14430.1589-0.0417-0.34310.05310.01610.0214-0.02380.3566-0.01330.1135-40.1785-24.7538-24.0892
60.74940.44460.3741.08280.40130.82670.03980.1149-0.16370.0019-0.0018-0.10710.16610.1113-0.03810.04210.03620.00590.10610.00050.0506-1.1631-29.1066-8.4074
72.06570.32971.38834.90181.10891.663-0.05790.04190.592-0.0284-0.0463-0.5374-0.48260.38610.10420.4106-0.18660.19830.38380.01070.388725.627569.431161.6628
81.30610.08891.00243.7126-0.60862.23730.0235-0.08760.47580.1129-0.0385-0.4192-0.39210.64660.0150.1182-0.19570.12690.6584-0.12910.423542.508963.295584.879
90.8705-0.36550.42210.5541-0.09861.18490.0593-0.08-0.1147-0.09860.0579-0.01450.12760.0636-0.11720.1279-0.02690.03850.10180.0270.06288.340844.371168.9007
102.79740.83911.29763.28050.50592.4235-0.0438-0.45380.44740.35330.0121-0.1555-0.3883-0.09350.03170.40470.03140.18260.20460.01040.3105-22.79491.505869.9482
111.48340.5051.54071.386-0.28913.7356-0.0856-0.01440.5140.11460.0261-0.2061-0.38020.01490.05940.52720.09340.16540.16370.03660.6935-28.5621117.583857.688
120.9222-0.250.47120.7076-0.35040.8796-0.00170.12670.1571-0.04280.07210.2076-0.0403-0.1646-0.07040.20040.00560.11070.12890.0890.2109-25.956878.855941.3864
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 166
2X-RAY DIFFRACTION2A179 - 462
3X-RAY DIFFRACTION3B2 - 777
4X-RAY DIFFRACTION4C1 - 166
5X-RAY DIFFRACTION5C179 - 462
6X-RAY DIFFRACTION6D2 - 777
7X-RAY DIFFRACTION7E1 - 166
8X-RAY DIFFRACTION8E179 - 462
9X-RAY DIFFRACTION9F2 - 777
10X-RAY DIFFRACTION10G1 - 166
11X-RAY DIFFRACTION11G179 - 462
12X-RAY DIFFRACTION12H2 - 777

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